期刊
BIOMOLECULAR NMR ASSIGNMENTS
卷 15, 期 2, 页码 415-420出版社
SPRINGER
DOI: 10.1007/s12104-021-10039-2
关键词
NMR resonance assignment; Decorin-binding proteins; Borrelia afzelii
资金
- Johannes Kepler University Linz
- Ministry of Education, Youth and Sports of the Czech Republic [LTARF18021, LTAUSA18040]
- Grant Agency of the Czech Republic [18-27204S]
- European Union, program EFRE INTERREG IV ETC-AT-CZ [M00146]
- regional OeAD grant [WTZ AT-CZ 11/2020]
In this study, the interaction of various European Borrelia spirochetes and their Dbp proteins was investigated using NMR, with a focus on B. afzelii DbpA. By predicting secondary structure propensity and analyzing backbone dynamics, structural differences of B. afzelii DbpA compared to other species were identified and will be further explored to understand their impact on host interactions.
Decorin binding proteins (Dbps) mediate attachment of spirochetes in host organisms during the early stages of Lyme disease infection. Previously, different binding mechanisms of Dbps to glycosaminoglycans have been elucidated for the pathogenic species Borrelia burgdorferi sensu stricto and B. afzelii. We are investigating various European Borrelia spirochetes and their interactions at the atomic level using NMR. We report preparative scale recombinant expression of uniformly stable isotope enriched B. afzelii DbpA in Escherichia coli, its chromatographic purification, and solution NMR assignments of its backbone and sidechain H-1, C-13, and N-15 atoms. This data was used to predict secondary structure propensity, which we compared to the North American B. burgdorferi sensu stricto and European B. garinii DbpA for which solution NMR structures had been determined previously. Backbone dynamics of DbpA from B. afzelii were elucidated from spin relaxation and heteronuclear NOE experiments. NMR-based secondary structure analysis together with the backbone dynamics characterization provided a first look into structural differences of B. afzelii DbpA compared to the North American species and will serve as the basis for further investigation of how these changes affect interactions with host components.
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